Structural and Biochemical Analysis Reveals Catalytic Mechanism of Fucoidan Lyase from Flavobacterium sp. SA-0082
文献类型：期刊论文
| 作者 | Wang, Juanjuan1,2; Liu, Zebin3,4; Pan, Xiaowei2,4; Wang, Ning2; Li, Legong4; Du, Yuguang3; Li, Jianjun3; Li, Mei2 |
| 刊名 | MARINE DRUGS
 |
| 出版日期 | 2022-08-01 |
| 卷号 | 20期号:8页码:20 |
| 关键词 | fucoidan lyase polysaccharides crystal structure catalytic mechanism |
| DOI | 10.3390/md20080533 |
| 英文摘要 | Fucoidans represent a type of polyanionic fucose-containing sulfated polysaccharides (FCSPs) that are cleaved by fucoidan-degrading enzymes, producing low-molecular-weight fucoidans with multiple biological activities suitable for pharmacological use. Most of the reported fucoidan-degrading enzymes are glycoside hydrolases, which have been well studied for their structures and catalytic mechanisms. Little is known, however, about the rarer fucoidan lyases, primarily due to the lack of structural information. FdlA from Flavobacterium sp. SA-0082 is an endo-type fucoidan-degrading enzyme that cleaves the sulfated fuco-glucuronomannan (SFGM) through a lytic mechanism. Here, we report nine crystal structures of the catalytic N-terminal domain of FdlA (FdlA-NTD), in both its wild type (WT) and mutant forms, at resolutions ranging from 1.30 to 2.25 angstrom. We show that the FdlA-NTD adopts a right-handed parallel beta-helix fold, and possesses a substrate binding site composed of a long groove and a unique alkaline pocket. Our structural, biochemical, and enzymological analyses strongly suggest that FdlA-NTD utilizes catalytic residues different from other beta-helix polysaccharide lyases, potentially representing a novel polysaccharide lyase family. |
| WOS关键词 | SULFATED POLYSACCHARIDES ; CRYSTAL-STRUCTURE ; ALGINATE LYASE ; BROWN ; CLASSIFICATION ; PURIFICATION ; SUBSITES ; PRODUCT ; STRAIN |
| 资助项目 | Strategic Priority Research Program of CAS[XDB27020106] ; National Natural Science Foundation of China[21877114] ; National Natural Science Foundation of China[31930064] |
| WOS研究方向 | Pharmacology & Pharmacy |
| 语种 | 英语 |
| WOS记录号 | WOS:000845465900001 |
| 出版者 | MDPI |
| 资助机构 | Strategic Priority Research Program of CAS ; National Natural Science Foundation of China |
| 源URL | [http://ir.ipe.ac.cn/handle/122111/54609]  |
| 专题 | 中国科学院过程工程研究所 |
| 通讯作者 | Li, Jianjun; Li, Mei |
| 作者单位 | 1.Univ Sci & Technol China, Div Life Sci & Med, Hefei 230027, Peoples R China 2.Chinese Acad Sci, Inst Biophys, CAS Ctr Excellence Biomacromol, Natl Lab Biomacromol, Beijing 100101, Peoples R China 3.Chinese Acad Sci, Inst Proc Engn, State Key Lab Biochem Engn, Beijing 100190, Peoples R China 4.Capital Normal Univ, Coll Life Sci, Beijing 100101, Peoples R China |
| 推荐引用方式 GB/T 7714 | Wang, Juanjuan,Liu, Zebin,Pan, Xiaowei,et al. Structural and Biochemical Analysis Reveals Catalytic Mechanism of Fucoidan Lyase from Flavobacterium sp. SA-0082[J]. MARINE DRUGS,2022,20(8):20. |
| APA | Wang, Juanjuan.,Liu, Zebin.,Pan, Xiaowei.,Wang, Ning.,Li, Legong.,...&Li, Mei.(2022).Structural and Biochemical Analysis Reveals Catalytic Mechanism of Fucoidan Lyase from Flavobacterium sp. SA-0082.MARINE DRUGS,20(8),20. |
| MLA | Wang, Juanjuan,et al."Structural and Biochemical Analysis Reveals Catalytic Mechanism of Fucoidan Lyase from Flavobacterium sp. SA-0082".MARINE DRUGS 20.8(2022):20. |
入库方式： OAI收割
来源：过程工程研究所
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